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Publication : RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling.

First Author  Chen CK Year  1996
Journal  Proc Natl Acad Sci U S A Volume  93
Issue  23 Pages  12885-9
PubMed ID  8917514 Mgi Jnum  J:36569
Mgi Id  MGI:83997 Doi  10.1073/pnas.93.23.12885
Citation  Chen CK, et al. (1996) RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. Proc Natl Acad Sci U S A 93(23):12885-9
abstractText  G proteins regulate intracellular signaling by coupling a cycle of guanine nucleotide binding and hydrolysis to transient changes of cellular functions. The mechanisms that control the recycling of transducin, the pacesetting G protein that regulates mammalian phototransduction, are unclear. We show that a novel retinal specific RGS-motif protein specifically binds to an intermediate conformation involved in GTP hydrolysis by transducin and accelerates phosphate release and the recycling of transducin. This specific interaction further rationalizes the kinetics of the phototransduction cascade and provides a general hypothesis to explain the mechanism of interaction of RGS proteins with other G proteins.
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